A tryptophan synchronous and normal fluorescence study on bacteria inactivation mechanism.

Abstract:

:The UV photodissociation kinetics of tryptophan amino acid, Trp, attached to the membrane of bacteria, Escherichia coli and Bacillus subtilis, have been studied by means of normal and synchronous fluorescence. Our experimental data suggest that the fluorescence intensity of Trp increases during the first minute of irradiation with 250 nm to ∼ 280 nm, 7 mW/cm2 UV light, and subsequently decreases with continuous irradiation. During this short, less than a minute, period of time, 70% of the 107 cell per milliliter bacteria are inactivated. This increase in fluorescence intensity is not observed when tryptophan is in the free state, namely, not attached to a protein, but dissolved in water or saline solution. This increase in fluorescence is attributed to the additional fluorescence of tryptophan molecules formed by protein unfolding, the breakage of the bond that attaches Trp to the bacterial protein membrane, or possibly caused by the irradiation of 2 types of tryptophan residues that photolyze with different quantum yields.

authors

Li R,Dhankhar D,Chen J,Cesario TC,Rentzepis PM

doi

10.1073/pnas.1909722116

subject

Has Abstract

pub_date

2019-09-17 00:00:00

pages

18822-18826

issue

38

eissn

0027-8424

issn

1091-6490

pii

1909722116

journal_volume

116

pub_type

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